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Database: UniProt
Entry: O57382
LinkDB: O57382
Original site: O57382 
ID   TLL2_XENLA              Reviewed;        1019 AA.
AC   O57382;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JAN-2019, entry version 93.
DE   RecName: Full=Tolloid-like protein 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Metalloprotease xolloid;
DE   AltName: Full=Xenopus tolloid;
DE   Flags: Precursor;
GN   Name=tll2; Synonyms=xld;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Ovary;
RX   PubMed=9520331; DOI=10.1006/dbio.1997.8840;
RA   Goodman S.A., Albano R., Wardle F.C., Matthews G., Tannahill D.,
RA   Dale L.;
RT   "BMP1-related metalloproteinases promote the development of ventral
RT   mesoderm in early Xenopus embryos.";
RL   Dev. Biol. 195:144-157(1998).
CC   -!- FUNCTION: Protease which specifically processes prolysyl oxidase
CC       and maybe also chordin. Required for the embryonic development.
CC       Predominant protease, which in the development, influences dorsal-
CC       ventral patterning and skeletogenesis. In embryos, inhibits the
CC       development of dorsoanterior structures and ventralizes activin-
CC       induced dorsal mesoderm in animal caps.
CC       {ECO:0000269|PubMed:9520331}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9520331}.
CC   -!- DEVELOPMENTAL STAGE: Initial uniform expression becomes localized
CC       to two posterior ectodermal patches flanking the neural plate and
CC       later to the inner ectoderm of the developing tailbud. Also
CC       expressed in dorsal regions of the brain during tailbud stages and
CC       is especially abundant in the ventricular layer of the dorsal
CC       hindbrain caudal to the otic vesicle.
CC       {ECO:0000269|PubMed:9520331}.
DR   EMBL; Y09661; CAA70854.1; -; mRNA.
DR   RefSeq; NP_001084377.1; NM_001090908.1.
DR   UniGene; Xl.36; -.
DR   ProteinModelPortal; O57382; -.
DR   SMR; O57382; -.
DR   MEROPS; M12.015; -.
DR   PRIDE; O57382; -.
DR   GeneID; 399469; -.
DR   KEGG; xla:399469; -.
DR   CTD; 399469; -.
DR   Xenbase; XB-GENE-478934; tll2.
DR   HOVERGEN; HBG004859; -.
DR   KO; K13047; -.
DR   OrthoDB; 170905at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 5.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 5.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR015446; BMP_1/tolloid-like.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR034036; ZnMP_TLD/BMP1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 5.
DR   Pfam; PF00008; EGF; 1.
DR   PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 5.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 5.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cleavage on pair of basic residues; Developmental protein;
KW   Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Repeat; Secreted;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   PROPEP       32    152       {ECO:0000250}.
FT                                /FTId=PRO_0000046040.
FT   CHAIN       153   1019       Tolloid-like protein 2.
FT                                /FTId=PRO_0000046041.
FT   DOMAIN      153    352       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      354    466       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      467    579       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      579    620       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      623    735       CUB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      735    775       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      779    891       CUB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      892   1008       CUB 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   ACT_SITE    246    246       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       245    245       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       249    249       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       255    255       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD    174    174       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    364    364       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    395    395       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    631    631       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    195    351       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    215    237       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    217    218       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    354    380       {ECO:0000250}.
FT   DISULFID    407    429       {ECO:0000250}.
FT   DISULFID    467    493       {ECO:0000250}.
FT   DISULFID    520    542       {ECO:0000250}.
FT   DISULFID    583    595       {ECO:0000250}.
FT   DISULFID    591    604       {ECO:0000250}.
FT   DISULFID    606    619       {ECO:0000250}.
FT   DISULFID    623    649       {ECO:0000250}.
FT   DISULFID    676    698       {ECO:0000250}.
FT   DISULFID    739    750       {ECO:0000250}.
FT   DISULFID    746    759       {ECO:0000250}.
FT   DISULFID    761    774       {ECO:0000250}.
FT   DISULFID    779    805       {ECO:0000250}.
FT   DISULFID    832    854       {ECO:0000250}.
FT   DISULFID    892    922       {ECO:0000250}.
FT   DISULFID    949    971       {ECO:0000250}.
SQ   SEQUENCE   1019 AA;  114892 MW;  50CCE8B7E3B42C6E CRC64;
     MSCGSPQVMM TLWTLTCVGL ILLGAIRLSL GLDYDLESFD YLMEDNPEEF DYKDPCKAAA
     YWGDIALDED DLKWIFKNKS NDLRNTRHNQ THPTTDNFSE KLGTGSQNET SSNLNSKKVK
     KGSRLKLLIA EKAATETNST FQVQTSNDRV RRAATSRTER IWPGGIIPYA IAGNFTGTQR
     AIFKQAMRHW KKHTCVTFVE RTDEESFIVF TYRPCGCCSY VGRRGGGPQA ISIGKNCDKF
     GIVVHELGHV VGFWHEHTRP DRDEHVSIIR ENIQPGQEYN FLKMEPGEVS SLGETYDFDS
     IMHYARNTFS RGVFLDTILP RRIDTSVRPT IGQRIRLSQG DIAQAKKLYK CPACGETLQD
     SSGNFSAPGY PSGYPSYTHC IWRISVTPGE KIILNFTTMD LFKSRLCWYD YIEIRDGYWR
     KAALLGRLCG DKLPDPIISS DSKLWIEFRS SSNILGKGFF AAYEAICGGD IKKDSGQIQS
     PNYPDDYRPA KECIWKITVS EGFLVGLSFQ AFEIERHDNC AYDYLEVRDG FSEDHALIGR
     FCGYEKPEDI KSTSNKLWIK FASDGSINKA GFSANFFKEM DECSRPDNGG CSQRCVNTLG
     SYKCVCEPGF ELTADKKSCE AACGGFITQL NGTITSPGWP KEYPTNKNCV WQVVAPAQYR
     ISLQFEVFEL EGNDVCKYDY LEIRSGLSSE SKLHGKFCGP EKPEVITSQG NTVRIEFKSD
     NTVSKKGFKA NFFSDKDECS KDNGGCQHDC VNTFGSYICQ CKNGFILHEN GHDCKEAGCE
     QKLLNAEGTI SSPNWPEKYP SRKECTWDIS VTAGHRVKLV FTDFEIEQHQ ECAYDHLELY
     DGPNGKAAIL GRFCGSKEPS PVVASTNNMF LRFYSDASVQ RKGFQAKYSP ECGGRLKAEI
     QTNDIYSHAQ FGDNNYPVQS NCEWVIVAED GYGVELIFQT FEIEEESDCG YDYMEVYDGY
     DSTAPRLGRY CGSGPPEEMY SAGDSIMIRF HTDDTINKKG FHGQYTSTKF QDALHMRRK
//
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